1knc: Difference between revisions
New page: left|200px<br /><applet load="1knc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1knc, resolution 2.00Å" /> '''Structure of AhpD fr... |
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[[Image:1knc.gif|left|200px]]<br /><applet load="1knc" size=" | [[Image:1knc.gif|left|200px]]<br /><applet load="1knc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1knc, resolution 2.00Å" /> | caption="1knc, resolution 2.00Å" /> | ||
'''Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.'''<br /> | '''Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.'''<br /> | ||
==Overview== | ==Overview== | ||
Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against | Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense. | ||
==About this Structure== | ==About this Structure== | ||
1KNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1KNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bryk, R.]] | [[Category: Bryk, R.]] | ||
[[Category: Erdjument-Bromage, H.]] | [[Category: Erdjument-Bromage, H.]] | ||
[[Category: Lima, C | [[Category: Lima, C D.]] | ||
[[Category: Nathan, C.]] | [[Category: Nathan, C.]] | ||
[[Category: Tempst, P.]] | [[Category: Tempst, P.]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:56 2008'' | ||
Revision as of 14:35, 21 February 2008
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Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.
OverviewOverview
Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense.
About this StructureAbout this Structure
1KNC is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein., Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C, Science. 2002 Feb 8;295(5557):1073-7. Epub 2002 Jan 17. PMID:11799204
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